Regulation of Cav1.2 current: interaction with intracellular molecules

J Pharmacol Sci. 2007 Apr;103(4):347-53. doi: 10.1254/jphs.cr0070012. Epub 2007 Apr 4.

Abstract

Ca(V)1.2 (alpha(1c)) is a pore-forming subunit of the voltage-dependent L-type calcium channel and is expressed in many tissues. The beta and alpha(2)/delta subunits are auxiliary subunits that affect the kinetics and the expression of Ca(V)1.2. In addition to the beta and alpha(2)/delta subunits, several molecules have been reported to be involved in the regulation of Ca(V)1.2 current. Calmodulin, CaBP1 (calcium-binding protein-1), CaMKII (calcium/calmodulin-dependent protein kinase II), AKAPs (A-kinase anchoring proteins), phosphatases, Caveolin-3, beta(2)-adrenergic receptor, PDZ domain proteins, sorcin, SNARE proteins, synaptotagmin, CSN5, RGK family, and AHNAK1 have all been reported to interact with Ca(V)1.2 and the beta subunit. This review focuses on the effect of these molecules on Ca(V)1.2 current.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcium Channels, L-Type / genetics
  • Calcium Channels, L-Type / metabolism
  • Calcium Channels, L-Type / physiology*
  • Calcium-Binding Proteins / metabolism
  • Calcium-Binding Proteins / physiology
  • Humans
  • Membrane Potentials / physiology
  • Molecular Sequence Data
  • Protein Binding
  • Sequence Homology, Amino Acid
  • Signal Transduction / physiology*

Substances

  • Calcium Channels, L-Type
  • Calcium-Binding Proteins
  • L-type calcium channel alpha(1C)
  • Ca2+-binding protein-1